ID A0A2G8LDW7_STIJA Unreviewed; 724 AA.
AC A0A2G8LDW7;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Xaa-Pro aminopeptidase 1 {ECO:0008006|Google:ProtNLM};
GN ORFNames=BSL78_04638 {ECO:0000313|EMBL:PIK58417.1};
OS Stichopus japonicus (Sea cucumber).
OC Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Holothuroidea;
OC Aspidochirotacea; Aspidochirotida; Stichopodidae; Apostichopus.
OX NCBI_TaxID=307972 {ECO:0000313|EMBL:PIK58417.1, ECO:0000313|Proteomes:UP000230750};
RN [1] {ECO:0000313|EMBL:PIK58417.1, ECO:0000313|Proteomes:UP000230750}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Shaxun {ECO:0000313|EMBL:PIK58417.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:PIK58417.1};
RX PubMed=29023486;
RA Zhang X., Sun L., Yuan J., Sun Y., Gao Y., Zhang L., Li S., Dai H.,
RA Hamel J.F., Liu C., Yu Y., Liu S., Lin W., Guo K., Jin S., Xu P.,
RA Storey K.B., Huan P., Zhang T., Zhou Y., Zhang J., Lin C., Li X., Xing L.,
RA Huo D., Sun M., Wang L., Mercier A., Li F., Yang H., Xiang J.;
RT "The sea cucumber genome provides insights into morphological evolution and
RT visceral regeneration.";
RL PLoS Biol. 15:E2003790-E2003790(2017).
CC -!- SIMILARITY: Belongs to the peptidase M24B family.
CC {ECO:0000256|ARBA:ARBA00008766}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PIK58417.1}.
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DR EMBL; MRZV01000113; PIK58417.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G8LDW7; -.
DR STRING; 307972.A0A2G8LDW7; -.
DR Proteomes; UP000230750; Unassembled WGS sequence.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR CDD; cd01085; APP; 1.
DR Gene3D; 3.90.230.10; Creatinase/methionine aminopeptidase superfamily; 1.
DR Gene3D; 3.40.350.10; Creatinase/prolidase N-terminal domain; 2.
DR InterPro; IPR029149; Creatin/AminoP/Spt16_NTD.
DR InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR InterPro; IPR000587; Creatinase_N.
DR InterPro; IPR000994; Pept_M24.
DR InterPro; IPR033740; Pept_M24B.
DR InterPro; IPR032416; Peptidase_M24_C.
DR PANTHER; PTHR43763; XAA-PRO AMINOPEPTIDASE 1; 1.
DR PANTHER; PTHR43763:SF6; XAA-PRO AMINOPEPTIDASE 1; 1.
DR Pfam; PF01321; Creatinase_N; 1.
DR Pfam; PF16189; Creatinase_N_2; 1.
DR Pfam; PF00557; Peptidase_M24; 1.
DR Pfam; PF16188; Peptidase_M24_C; 1.
DR SUPFAM; SSF55920; Creatinase/aminopeptidase; 1.
DR SUPFAM; SSF53092; Creatinase/prolidase N-terminal domain; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000230750}.
FT DOMAIN 62..193
FT /note="Creatinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01321"
FT DOMAIN 393..619
FT /note="Peptidase M24"
FT /evidence="ECO:0000259|Pfam:PF00557"
FT DOMAIN 631..691
FT /note="Peptidase M24 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16188"
SQ SEQUENCE 724 AA; 81801 MW; C04DFD727CBE3E8F CRC64;
MHRRLAQWPI LHLVTSSPIE AGHDANIALP KQRVRRQDES VRDCTAVPPT YPETTVMTDE
QLLKLREYMD LNDIEAYIIP SEDAHQSEYI AEADERRLFV SGFDGSAGLA IVTTNRAAVW
VDGRYFLQAK MQLDCNWVSQ EIGEPNVPSP ADWLLAESTD EGLGASLSSG AKVGFDPTLL
SISTYFSYNE TFEASDRGIM LQSIEDNLVD RIWVDMEGEK PAYPGDELLI LEHEYTGRTW
EEKIFDTSAG YDTIRELMAE KDADALVVTK LDEIAWIFNL RGADIPYNPM FISYAIIETD
AIKLYLYDMT TRAVQEIEDH LKQGSCTPTA NCITIKDYDA FLGDLEDIGS TKKVWHSDTG
SYAIYERVAE DNRIMEASPI LLMKARKNPT EMEGLRQACK KDSISLCELF GWIQEKVDAM
TDEQATTGDL TYLSELIIED EAYKVRERWG HEFTGHSFKS ISAFAEHGAI IHYSSSETTD
VPVTKQGTYM LDSGSQFKDG TTDITRTLHY GTPTAFEKEA YTRVLMGHID LVNTNFRSGV
YGRDIDAIAR EPLWSNGLDY RHGTGHGIGH FLNVHEGPIN IGNYPGEQPM QTGVFLSDEP
GYYEDGSFGI RLENDMIVVD AVTDHSFSTY EYMTFEMISL VPFDPNLIDF TMLSPAQLEW
YNVYTERVRN EIGPALSDRA RNWMERNTYP IEYTFTVNSG STEPLSVLMT ATCLIISVRL
LNLY
//